Related references
Note: Only part of the references are listed.You've come a long way: c-di-GMP signaling
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Solution Structure of the PilZ Domain Protein PA4608 Complex with Cyclic di-GMP Identifies Charge Clustering as Molecular Readout
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MrkH, a Novel c-di-GMP-Dependent Transcriptional Activator, Controls Klebsiella pneumoniae Biofilm Formation by Regulating Type 3 Fimbriae Expression
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The Cyclic Nucleotide Monophosphate Domain of Xanthomonas campestris Global Regulator Clp Defines a New Class of Cyclic Di-GMP Effectors
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Bistable Expression of CsgD in Biofilm Development of Salmonella enterica Serovar Typhimurium
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The cAMP Receptor-Like Protein CLP Is a Novel c-di-GMP Receptor Linking Cell-Cell Signaling to Virulence Gene Expression in Xanthomonas campestris
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JOURNAL OF MOLECULAR BIOLOGY (2010)
Structure of PP4397 Reveals the Molecular Basis for Different c-di-GMP Binding Modes by Pilz Domain Proteins
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The c-di-GMP Binding Protein YcgR Controls Flagellar Motor Direction and Speed to Affect Chemotaxis by a Backstop Brake Mechanism
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Genetic reductionist approach for dissecting individual roles of GGDEF proteins within the c-di-GMP signaling network in Salmonella
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Structural Analysis of the GGDEF-EAL Domain-Containing c-di-GMP Receptor FimX
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Identification of FleQ from Pseudomonas aeruginosa as a c-di-GMP-responsive transcription factor
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A comprehensive genetic characterization of bacterial motility
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A cyclic-di-GMP receptor required for bacterial exopolysaccharide production
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The second messenger bis-(3′-5′)-cyclic-GMP and its PilZ domain-containing receptor Alg44 are required for alginate biosynthesis in Pseudomonas aeruginosa
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PilZ domain proteins bind cyclic diguanylate and regulate diverse processes in Vibrio cholerae
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DgrA is a member of a new family of cyclic diguanosine monophosphate receptors and controls flagellar motor function in Caulobacter crescentus
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NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein
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c-di-GMP-mediated regulation of virulence and biofilm formation
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Allosteric control of cyclic di-GMP signaling
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The PilZ domain is a receptor for the second messenger c-di-GMP - The PilZ domain protein YcgR controls motility in enterobacteria
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Cell-cell signaling in Xanthomonas campestris involves an HD-GYP domain protein that functions in cyclic di-GMP turnover
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Cyclic di-GMP as a second messenger
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PilZ domain is part of the bacterial c-di-GMP binding protein
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R Simm et al.
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The EAL domain protein VieA is a cyclic diguanylate phosphodiesterase
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Identification and characterization of a cyclic di-GMP-specific phosphodiesterase and its allosteric control by GTP
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The ubiquitous protein domain EAL is a cyclic diguanylate-specific phosphodiesterase: Enzymatically active and inactive EAL domains
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Exopolysaccharide sugars contribute to biofilm formation by Salmonella enterica serovar typhimurium on HEp-2 cells and chicken intestinal epithelium
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Cyclic diguanylate is a ubiquitous signaling molecule in bacteria: Insights into biochemistry of the GGDEF protein domain
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Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain
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Role of the GGDEF protein family in Salmonella cellulose biosynthesis and biofilm formation
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Structure of the constitutively active double mutant cheYD13K Y106W alone and in complex with a flim peptide
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GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility
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Structural basis of activity and allosteric control of diguanylate cyclase
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Comparative analysis of Salmonella enterica serovar typhimurium biofilm formation on gallstones and on glass
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The multicellular morphotypes of Salmonella typhimurium and Escherichia coli produce cellulose as the second component of the extracellular matrix
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